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Cathepsin L, But Not Cathepsin B, Is a Potential Kininogenase

Cathepsin L, But Not Cathepsin B, Is a Potential Kininogenase Abstract Although papainlike enzymes are strongly inhibited by their natural tightbinding inhibitors of the cystatin superfamily, cathepsins B and L may still retain some residual proteolytic activity toward ZPheArgAMC in the presence of an excess of kininogen. This activity is abolished by adding E-64 or chicken cystatin. Cathepsins B and L show a single band of gelatinolytic activity when subjected to gelatinSDSPAGE. Adding high M kininogen, low M kininogen, Tkininogen, or chicken cystatin to cathepsin L results in additional intense bands of enzyme activity corresponding to the proteaseinhibitor complexes. Cathepsin B does not produce these additional bands. This gelatinolytic activity was inhibited by E-64, but not by EDTA, PMSF or Pefabloc. Cathepsin L also specifically generated kinins from high and low molecular weight kininogens in vitro, but cathepsin B did not. Tkininogen did not release any immunoreactive kinins when complexed with cathepsin L, as previously observed using tissue kallikreins. The ability of cathepsin L to generate vasoactive peptides raises the question of the physiological significance of this mechanism during inflammation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biological Chemistry de Gruyter

Cathepsin L, But Not Cathepsin B, Is a Potential Kininogenase

Biological Chemistry , Volume 382 (5) – May 5, 2001

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References (28)

Publisher
de Gruyter
Copyright
Copyright © 2001 by the
ISSN
1431-6730
DOI
10.1515/BC.2001.098
pmid
11517935
Publisher site
See Article on Publisher Site

Abstract

Abstract Although papainlike enzymes are strongly inhibited by their natural tightbinding inhibitors of the cystatin superfamily, cathepsins B and L may still retain some residual proteolytic activity toward ZPheArgAMC in the presence of an excess of kininogen. This activity is abolished by adding E-64 or chicken cystatin. Cathepsins B and L show a single band of gelatinolytic activity when subjected to gelatinSDSPAGE. Adding high M kininogen, low M kininogen, Tkininogen, or chicken cystatin to cathepsin L results in additional intense bands of enzyme activity corresponding to the proteaseinhibitor complexes. Cathepsin B does not produce these additional bands. This gelatinolytic activity was inhibited by E-64, but not by EDTA, PMSF or Pefabloc. Cathepsin L also specifically generated kinins from high and low molecular weight kininogens in vitro, but cathepsin B did not. Tkininogen did not release any immunoreactive kinins when complexed with cathepsin L, as previously observed using tissue kallikreins. The ability of cathepsin L to generate vasoactive peptides raises the question of the physiological significance of this mechanism during inflammation.

Journal

Biological Chemistryde Gruyter

Published: May 5, 2001

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